Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5398769 | Journal of Luminescence | 2015 | 30 Pages |
Abstract
Quantum dots (QDs) are a kind of nanostructured semiconductor crystals with the size range of 1-10Â nm. Their unique photophysical properties and potential toxicity to human health have aroused wide concern of scientists and general public. However, the interaction mechanism of QDs on human serum albumin (HSA, the vital protein in human blood) from both structural and functional perspectives is rarely reported. In the present work, effects of N-acetyl-L-cysteine-capped CdTe quantum dots with fluorescence emission peak at 612Â nm (QDs-612) on the conformation and function of HSA were investigated by spectroscopic methods, molecular docking study and esterase activity assay. The hydrophobic interaction between HSA and QDs-612 was spontaneous with the binding constants calculated to be 6.85Ã105Â LÂ molâ1 (298Â K) and 8.89Ã105Â LÂ molâ1 (308Â K). The binding of QDs-612 to HSA induced the static quenching of fluorescence and the changes of secondary structure and microenvironment of Tyr-411 residue, which resulted in serious decrease on the hydrolysis of substrate p-nitrophenylacetate in esterase activity assay of HSA. This work confirms the possibility on direct interaction of QDs-612 with HSA and obtains a possible mechanism of relationship between conformation and function of HSA.
Related Topics
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Physical and Theoretical Chemistry
Authors
Haoyu Sun, Xudan Yang, Meng Li, Songlin Han, Yingxue Liu, Xuejie Tan, Chunguang Liu, Rutao Liu,